초록
<P><B>Abstract</B><P>Background<P>As a cost-effective and eco-friendly approach, biocatalysis has great potential for the transformation of 5-hydroxymethylfurfural (HMF) into 2,5-furandicarboxylic acid (FDCA). However, the compatibility of each enzyme in the cascade reaction limits the transformation efficiency of HMF to FDCA.</P></P><P>Results<P>Coupled with an alcohol oxidase from <I>Colletotrichum gloeosporioides</I> (<I>Cgl</I>AlcOx), this study aims to study the potential of bacterial laccase from <I>Bacillus pumilus</I> (<I>Bp</I>Lac) in an enzymatic cascade for 2,5-furandicarboxylic acid (FDCA) biosynthesis from 5-hydroxymethylfurfural (HMF). <I>Bp</I>Lac showed 100% selectivity for HMF oxidation and generated 5-hydroxymethyl-2-furancarboxylic acid (HMFCA). <I>Cgl</I>AlcOx was capable of oxidizing HMFCA to 2-formyl-5-furancarboxylic acid (FFCA). Both <I>Bp</I>Lac and <I>Cgl</I>AlcOx could oxidize FFCA to FDCA. At the 5 mM scale, a complete transformation of HMF with a 97.5% yield of FDCA was achieved by coupling <I>Bp</I>Lac with <I>Cgl</I>AlcOx in the cascade reaction. The FDCA productivity in the reaction was 5.3 mg/L/h. Notably, <I>Bp</I>Lac could alleviate the inhibitory effect of FFCA on <I>Cgl</I>AlcOx activity and boost the transformation efficiency of HMF to FDCA. Moreover, the reaction was scaled up to 40 times the volume, and FDCA titer reached 2.6 mM with a yield of 58.77% at 168 h.</P></P><P>Conclusions<P>This work provides a candidate and novel insight for better design of an enzymatic cascade in FDCA production.</P></P></P>